1LPH: LYS(B28)PRO(B29)-human insulin

LYS(B28)PRO(B29)-human insulin. Determined by X-ray diffraction at 2.3 Å resolution. Released 20 Jun 1996.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
4
Atoms
864
Mol. weight
11.9 kDa
Ligands
ZN, IPH
Released
20 Jun 1996

Explore 1LPH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LPH contains 10 α-helices and 3 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 1 β-strand

ElementResiduesLengthSheet
α-helix21
α-helix3-97
α-helix13-164
α-helix17-193
β-strand2011
Chain B: 3 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix9-1911
α-helix20-223
β-strand24-2631
α-helix27-293
Chain C: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2-65
α-helix13-164
Chain D: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix4-1815
β-strand24-2631

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
InsulinA, Cprotein21Homo sapiensP01308 (AlphaFold model)
InsulinB, Dprotein30Homo sapiensP01308 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>1LPH_1 INSULIN (chains A, C)
GIVEQCCTSICSLYQLENYCN
Sequence of entity 2 (B, D), FASTA
>1LPH_2 INSULIN (chains B, D)
FVNQHLCGSHLVEALYLVCGERGFFYTKPT

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
IPHPhenolC6 H6 O1

Water and common crystallization additives (CL) are not listed.

Primary citation

Role of C-terminal B-chain residues in insulin assembly: the structure of hexameric LysB28ProB29-human insulin. Ciszak, E., Beals, J.M., Frank, B.H. et al. Structure (1995) 3:615-622. DOI 10.1016/S0969-2126(01)00195-2 · PubMed

Other PDB entries of the same protein (UniProt P01308 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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